1KEL
CATALYTIC ANTIBODY 28B4 FAB FRAGMENT COMPLEXED WITH HAPTEN (1-[N-4'-NITROBENZYL-N-4'-CARBOXYBUTYLAMINO] METHYLPHOSPHONIC ACID)
Summary for 1KEL
| Entry DOI | 10.2210/pdb1kel/pdb |
| Descriptor | 28B4 FAB, 1-[N-4'-NITROBENZYL-N-4'-CARBOXYBUTYLAMINO]METHYLPHOSPHONIC ACID (3 entities in total) |
| Functional Keywords | sulfide oxidation, monooxygenase, oxygenation, fab, immunoglobulin, catalytic antibody |
| Biological source | Mus musculus (house mouse) More |
| Cellular location | Isoform Secreted: Secreted: P01868 |
| Total number of polymer chains | 2 |
| Total formula weight | 47732.10 |
| Authors | Hsieh-Wilson, L.C.,Schultz, P.G.,Stevens, R.C. (deposition date: 1996-04-16, release date: 1996-12-07, Last modification date: 2024-11-20) |
| Primary citation | Hsieh-Wilson, L.C.,Schultz, P.G.,Stevens, R.C. Insights into antibody catalysis: structure of an oxygenation catalyst at 1.9-angstrom resolution. Proc.Natl.Acad.Sci.USA, 93:5363-5367, 1996 Cited by PubMed Abstract: The x-ray crystal structures of the sulfide oxidase antibody 28B4 and of antibody 28B4 complexed with hapten have been solved at 2.2-angstrom and 1.9-angstrom resolution, respectively. To our knowledge, these structures are the highest resolution catalytic antibody structures to date and provide insight into the molecular mechanism of this antibody-catalyzed monooxygenation reaction. Specifically, the data suggest that entropic restriction plays a fundamental role in catalysis through the precise alignment of the thioether substrate and oxidant. The antibody active site also stabilizes developing charge on both sulfur and periodate in the transition state via cation-pi and electrostatic interactions, respectively. In addition to demonstrating that the active site of antibody 28B4 does indeed reflect the mechanistic information programmed in the aminophosphonic acid hapten, these high-resolution structures provide a basis for enhancing turnover rates through mutagenesis and improved hapten design. PubMed: 8643580DOI: 10.1073/pnas.93.11.5363 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.9 Å) |
Structure validation
Download full validation report
